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Crystal structure of bacillus subtilis penicillin binding protein 3

Analyse Crystal structure of bacillus subtilis penicillin binding protein 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7BN9
Type
protein
Length
1,208 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Penicillin-binding protein 3
EC
3.4.16.4
UniProt
P42971
Pockets
12 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APenicillin-binding protein 3 (EC 3.4.16.4)protein63033% helix, 26% strandP42971
BPenicillin-binding protein 3 (EC 3.4.16.4)protein57833% helix, 20% strandP42971

Pockets

12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111320.770.7983empty
28970.690.7586empty
3530.560.9024empty
42270.490.7530empty
51710.470.7620empty

Interfaces

1 interface between chains.

  • A–B · 884 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 7BN9 · Crystal Structure of Bacillus subtilis Penicillin Binding Protein 3 · the same entry in another collection · chain A against A, TM-score 1.00
  • P42971 · AlphaFold monomer V2.0 prediction for penicillin-binding protein 3 (P42971) · a predicted model of the same protein · chain B against A, TM-score 0.93

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